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Sensing and responding to oxidative stress through RsrA-sigma R in streptomyces

ReferenceP11071
Principal Investigator / Supervisor Professor Mark Buttner
Co-Investigators /
Co-Supervisors
Dr Mark Paget
Institution John Innes Centre
DepartmentJohn Innes Centre Department
Funding typeResearch
Value (£) 179,020
StatusCompleted
TypeResearch Grant
Start date 01/03/1999
End date 30/04/2003
Duration50 months

Abstract

We have identified two proteins sigma R and RsrA (an anti-sigma factor), that modulate expression of the thioredoxin system in response to oxidative stress in S. coelicolor. The objectives of the proposed work are: (i) to identify by site-directed mutagenesis which of the 7 Cys residues are involved in the formation of the intramolecular disulphide bond that inactivates RsrA; (ii) to confirm this assignment through MALDI-TOF spectroscopic analysis of tryptic peptides generated from the reduced and oxidised form of RsrA (from which the 5 other Cys residues have been removed); (iii) to confirm the in vitro biochemical data by examining the activity of the rsrA mutant alleles in vivo; (iv) to identify further genes under sigma R control; (v) to determine if oxidised RsrA is a substrate for the thioredoxin system; (vi) to examine the effect of up-regulating tr BA expression on the yield of the ACV-derived Beta-lactam cephamycin C in S. clavuligerus.

Summary

unavailable
Committee Closed Committee - Plant & Microbial Sciences (PMS)
Research TopicsX – not assigned to a current Research Topic
Research PriorityX – Research Priority information not available
Research Initiative X - not in an Initiative
Funding SchemeX – not Funded via a specific Funding Scheme
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